On the cover
The dynamin-related GTPase Drp1 (green) localizes in foci where it cleaves the mitochondrial network (red). Otera et al. demonstrate that the protein Mff is required for Drp1 recruitment and mitochondrial fission in mammalian cells. Image © 2010 Hidenori Otera.
See page 1141.
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In This Issue
People & Ideas
The cell biology of disease
Ino80 facilitates restoration of nucleosome structure during NER-mediated repair of UV-induced lesions.
Vesicle trafficking maintains nuclear shape in Saccharomyces cerevisiae during membrane proliferation
Disruption of vesicle trafficking results in distortion of nuclear shape and increased nuclear envelope surface area but doesn’t alter the nuclear/cell volume ratio.
Lte1 interacts with and inhibits the small GTPases Ras and Bud1, blocking polarization until mitosis is complete.
NADPH oxidase links endoplasmic reticulum stress, oxidative stress, and PKR activation to induce apoptosis
ER stress signaling involving calcium and CaMKII induces NADPH oxidase and oxidative stress, which amplify CHOP-mediated apoptosis via PKR activation.
Molecular architecture of a dynamin adaptor: implications for assembly of mitochondrial fission complexes
Structural and functional studies of the Mdv1 dimer reveal how this mitochondria-associated adaptor protein orients and stabilizes the assembly of dynamins on membranes to promote mitochondrial fission.
Mff is an essential factor for mitochondrial recruitment of Drp1 during mitochondrial fission in mammalian cells
Localization of the dynamin-related GTPase Drp1 to mitochondria relies on the mitochondrial fission factor Mff.
Formin follows function: a muscle-specific isoform of FHOD3 is regulated by CK2 phosphorylation and promotes myofibril maintenance
Phosphorylation of the muscle-specific formin splice variant FHOD3 by CK2 regulates its stability, myofibril targeting, and myofibril integrity.
RNAi screen identifies a role for adaptor protein AP-3 in sorting to the regulated secretory pathway
AP-3 concentrates proteins within large dense-core vesicles to promote regulated exocytosis.
Changes in protein tyrosine phosphatase 1B expression affect duration and amplitude of EphA3 phosphorylation and cell surface concentration.
Rather than passively binding ligands via immunoreceptors, macrophages capture particles by repeated extension of actin-rich protrusions.